Antigen bound antibody interacts with C1complement complex

Stable Identifier
R-GGA-2132064
Type
Reaction [binding]
Species
Gallus gallus
Compartment
ReviewStatus
5/5
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Complement protein C1q binds either to antibody-antigen complexes or directly to the surfaces of certain pathogens (Ebenbichier CF et al. 1991, Ikeda F et al. 1998, Spiller OB & Morgan BP 1998). C1q belongs to the family of collectins, which contain both lectin and collagen-like domains. It has six globular subunits linked by their collagen tails. Each of the six C1q subunits is composed of three polypeptide chains - A, B and C. The serine protease subunits C1r and C1s form a Ca2+-dependent C1s-C1r-C1r-C1s tetramer that is thought to be bent around the collageneous tail of C1q to form the C1 complex (Arlaud GJ et al. 2001).
Chicken C1q (chC1q) was purified from chicken serum. Like its human counterpart chC1q has a structure with six globular subunits. Sequences of chicken C1qA, C1qB and C1qC chains were identified on the same chromosome and show 44, 53 and 58% amino acid sequence identity to their human counterparts respectively. Chicken C1q was shown to generate full C1 hemolytic activity when assayed with human complement subcomponents C1r and C1s (Yonemasu & Sasaki 1986).
Predicted chicken C1s and C1r share 56% and 58% sequence identity with human C1s and C1r respectively.
Literature References
PubMed ID Title Journal Year
9815210 Antibody-independent activation of the classical complement pathway by cytomegalovirus-infected fibroblasts

Spiller, OB, Morgan, BP

J. Infect. Dis. 1998
3007627 Purification, identification and characterization of chicken C1q, a subcomponent of the first component of complement

Yonemasu, K, Sasaki, T

J. Immunol. Methods 1986
1744579 Human immunodeficiency virus type 1 activates the classical pathway of complement by direct C1 binding through specific sites in the transmembrane glycoprotein gp41

Vornhagen, R, Ebenbichler, CF, Arlaud, GJ, Marschang, P, Thielens, NM, Dierich, MP

J. Exp. Med. 1991
9820553 Human complement component C1q inhibits the infectivity of cell-free HTLV-I

Haraguchi, Y, Ikeda, F, Morishita, Y, Iino, Y, Shiraki, H, Hoshino, H, Jinno, A

J. Immunol. 1998
11414355 Structural biology of C1: dissection of a complex molecular machinery

Bersch, B, Arlaud, GJ, Gaboriaud, C, Rossi, V, Thielens, NM, Fontecilla-Camps, JC, Hernandez, JF

Immunol. Rev. 2001
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